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1MOW

E-DreI

1MOW の概要
エントリーDOI10.2210/pdb1mow/pdb
分子名称5'-D(*CP*CP*AP*AP*AP*CP*TP*GP*TP*CP*TP*CP*AP*AP*GP*TP*TP*CP*CP*GP*GP*CP*G)-3', 5'-D(*CP*GP*CP*CP*GP*GP*AP*AP*CP*TP*TP*GP*AP*GP*AP*CP*AP*GP*TP*TP*TP*GP*G)-3', chimera of homing endonuclease I-DmoI and DNA endonuclease I-CreI, ... (7 entities in total)
機能のキーワードlaglidadg, homing, engineering, design, endonuclease, hydrolase-dna complex, hydrolase/dna
由来する生物種Desulfurococcus mobilis (,)
詳細
細胞内の位置Plastid, chloroplast: p05725
タンパク質・核酸の鎖数12
化学式量合計179359.22
構造登録者
Chevalier, B.S.,Kortemme, T.,Chadsey, M.S.,Baker, D.,Monnat Jr., R.J.,Stoddard, B.L. (登録日: 2002-09-10, 公開日: 2002-11-29, 最終更新日: 2024-02-14)
主引用文献Chevalier, B.S.,Kortemme, T.,Chadsey, M.S.,Baker, D.,Monnat Jr., R.J.,Stoddard, B.L.
Design, Activity and Structure of a Highly Specific Artificial Endonuclease
Mol.Cell, 10:895-905, 2002
Cited by
PubMed Abstract: We have generated an artificial highly specific endonuclease by fusing domains of homing endonucleases I-DmoI and I-CreI and creating a new 1400 A(2) protein interface between these domains. Protein engineering was accomplished by combining computational redesign and an in vivo protein-folding screen. The resulting enzyme, E-DreI (Engineered I-DmoI/I-CreI), binds a long chimeric DNA target site with nanomolar affinity, cleaving it precisely at a rate equivalent to its natural parents. The structure of an E-DreI/DNA complex demonstrates the accuracy of the protein interface redesign algorithm and reveals how catalytic function is maintained during the creation of the new endonuclease. These results indicate that it may be possible to generate novel highly specific DNA binding proteins from homing endonucleases.
PubMed: 12419232
DOI: 10.1016/S1097-2765(02)00690-1
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.4 Å)
構造検証レポート
Validation report summary of 1mow
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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